Work on this project focuses on the origins of allosteric cooperativity in hemoglobins, the nature of changes in ligation of hemoglobins in hemoglobinopathies such as sickle cell anemia, the response of normal and abnormal erythrocytes to changing external conditions (such as oxygen tension, pH and DPG levels) and the molecular results of possible therapies such as hemoglobin carbamylation by isocyanate in sickle cell anemia. Magnetic resonance techniques particularly of C13 and P31 play an important role in these studies. BIBLIOGRAPHIC REFERENCES: Moon, Richard B., Dill, Killian and Richards, John H., Magnetic Resonance Studies of the Binding of C13 Carbon Monoxide to Myoglobins and Hemoglobins Containing Modified Hemes, in press Biochemistry (1976).